Glycan-binding agglutination assays reveal key binding epitope of unknown lectins in Acinetobacter baumannii
Abstract
Acinetobacter baumannii infections are associated with high mortality rates and an even higher prevalence of antimicrobial resistance. Understanding the lectin-glycan interactions mediating A. baumannii adhesion to cells will facilitate their exploitation in strategies to develop improved approaches to diagnosis and treatment. In this work, we use an established low-cost glycan-based agglutination assay to undertake a systematic structure-activity relationship screen of glycan ligands, and identify selective adhesion to α-GalNAc that is dependent upon both stereochemistry and presentation. Our work demonstrates how this approach can rapidly identify glycan motifs important to adhesion of understudied pathogens such as A. baumannii, information that is both therapeutically exploitable and furthers understanding of bacterial virulence.
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BibTeX
@misc{johns2026glycanbinding,
title = {{Glycan-binding agglutination assays reveal key binding epitope of unknown lectins in Acinetobacter baumannii}},
author = {Jennifer Johns and Charlene Mae Cagape and Narisara Chantratita and James Spencer and M. Carmen Galan},
howpublished = {ChemRxiv},
year = {2026},
month = sep,
doi = {10.26434/chemrxiv.15009048/v1},
url = {https://chemrxiv.org/doi/full/10.26434/chemrxiv.15009048/v1},
note = {CC BY},
}
RIS
TY - UNPB
TI - Glycan-binding agglutination assays reveal key binding epitope of unknown lectins in Acinetobacter baumannii
AU - Jennifer Johns
AU - Charlene Mae Cagape
AU - Narisara Chantratita
AU - James Spencer
AU - M. Carmen Galan
PY - 2026
DA - 2026/09/18
PB - ChemRxiv
DO - 10.26434/chemrxiv.15009048/v1
UR - https://chemrxiv.org/doi/full/10.26434/chemrxiv.15009048/v1
AB - Acinetobacter baumannii infections are associated with high mortality rates and an even higher prevalence of antimicrobial resistance. Understanding the lectin-glycan interactions mediating A. baumannii adhesion to cells will facilitate their exploitation in strategies to develop improved approaches to diagnosis and treatment. In this work, we use an established low-cost glycan-based agglutination assay to undertake a systematic structure-activity relationship screen of glycan ligands, and identify selective adhesion to α-GalNAc that is dependent upon both stereochemistry and presentation. Our work demonstrates how this approach can rapidly identify glycan motifs important to adhesion of understudied pathogens such as A. baumannii, information that is both therapeutically exploitable and furthers understanding of bacterial virulence.
ER -